TRI44_PONAB
ID TRI44_PONAB Reviewed; 344 AA.
AC Q5R846;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Tripartite motif-containing protein 44;
GN Name=TRIM44;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in the process of differentiation and
CC maturation of neuronal cells (By similarity). May regulate the activity
CC of TRIM17 (By similarity). Is a negative regulator of PAX6 expression
CC (By similarity). {ECO:0000250|UniProtKB:Q96DX7}.
CC -!- SUBUNIT: Interacts (via coiled coil) with TRIM17 (via coiled coil).
CC {ECO:0000250|UniProtKB:Q96DX7}.
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DR EMBL; CR859908; CAH92064.1; -; mRNA.
DR RefSeq; NP_001126201.1; NM_001132729.2.
DR AlphaFoldDB; Q5R846; -.
DR STRING; 9601.ENSPPYP00000003851; -.
DR Ensembl; ENSPPYT00000056148; ENSPPYP00000034514; ENSPPYG00000003355.
DR GeneID; 100173169; -.
DR KEGG; pon:100173169; -.
DR CTD; 54765; -.
DR eggNOG; ENOG502RHR7; Eukaryota.
DR GeneTree; ENSGT00440000034605; -.
DR HOGENOM; CLU_070347_0_0_1; -.
DR InParanoid; Q5R846; -.
DR OMA; LREAYMW; -.
DR OrthoDB; 869824at2759; -.
DR TreeFam; TF333911; -.
DR Proteomes; UP000001595; Chromosome 11.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR000315; Znf_B-box.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00336; BBOX; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Metal-binding; Phosphoprotein; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..344
FT /note="Tripartite motif-containing protein 44"
FT /id="PRO_0000324098"
FT ZN_FING 174..215
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 290..325
FT /evidence="ECO:0000255"
FT COMPBIAS 75..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..165
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXA7"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXA7"
SQ SEQUENCE 344 AA; 38456 MW; 595584AD36F2D691 CRC64;
MASGVGAAFE ELPHDGTCDE CEPDEAPGAE EVCRECGFCY CRRHAEAHRQ KFLSHHLAEY
VHGAQAWTPP ADGEGAGKEE AEVKVEQERE IESEAGEESE SEEESESEEE SETEEESEDE
SDEESEEDSE EEMEDEQESE AEEDNQEEGE SEAEGETEAE SEFDPEIEME AERVAKRKCP
DHGLDLSTYC QEDRQLICVL CPVIGAHQGH QLSTLDEAFE ELRSKDSGGL KAAMIELVER
LKFKSSDPKV TRDQMKMFIQ QEFKKVQKVI ADEEQKALHL VDIQEAMATA HVTEILADIQ
SHMDRLMTQM AQAKEQLDTS NESAEPKAEG DEEGPSGASE EEDT